Comparison of the effects of amino acid substitutions and β-N- vs. α-O-glycosylation on the T-cell stimulatory activity and conformation of an epitope on the rabies virus glycoprotein

BBA - Molecular Cell Research

Volumn 1267, Issue 1, 1995, Pages 55-64

  Otvos Jr , Laszlo ^a   Krivulka, Georgia R ^a   Urge, Laszlo ^a   Szendrei, Gyorgyi I ^a   Nagy, Laszlo ^a   Xiang, Zhi Q ^a   Ertl, Hildegund C J ^a  

^a WISTAR INSTITUTE   (United States)

Author keywords

Anomer; Circular dichroism; Class II major histocompatibility complex; Recognition

Indexed keywords

EPITOPE; VIRUS GLYCOPROTEIN;

ANIMAL CELL; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; RABIES VIRUS; STRUCTURE ACTIVITY RELATION; T LYMPHOCYTE ACTIVATION;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMAL; COMPARATIVE STUDY; EPITOPES; FEMALE; GLYCOPEPTIDES; GLYCOPROTEINS; GLYCOSYLATION; HISTOCOMPATIBILITY ANTIGENS; LYMPHOCYTE ACTIVATION; MICE; MICE, INBRED C3H; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; RABIES VIRUS; SUPPORT, U.S. GOV'T, P.H.S.; T-LYMPHOCYTES; VIRAL PROTEINS;

ANIMALIA; RABIES VIRUS;

EID: 0029012040     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/0167-4889(95)00030-V     Document Type: Article

References (56)

1. Rabies Subunit Vaccines
2. Glycosylation of synthetic T helper cell epitopic peptides influences their antigenic potency and conformation in a sugar location-specific manner
3. Circular dichroism of polypeptide solutions in the vacuum ultraviolet
4. Defining rules for the peptide-MHC class II interaction
5. Origin, structure and motifs of naturally processed MHC class II ligands